1jqp: Difference between revisions
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[[Image:1jqp.jpg|left|200px]] | [[Image:1jqp.jpg|left|200px]] | ||
'''dipeptidyl peptidase I (cathepsin C), a tetrameric cysteine protease of the papain family''' | {{Structure | ||
|PDB= 1jqp |SIZE=350|CAPTION= <scene name='initialview01'>1jqp</scene>, resolution 2.4Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_I Dipeptidyl-peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.1 3.4.14.1] | |||
|GENE= | |||
}} | |||
'''dipeptidyl peptidase I (cathepsin C), a tetrameric cysteine protease of the papain family''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1JQP is a [ | 1JQP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JQP OCA]. | ||
==Reference== | ==Reference== | ||
Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domain., Olsen JG, Kadziola A, Lauritzen C, Pedersen J, Larsen S, Dahl SW, FEBS Lett. 2001 Oct 12;506(3):201-6. PMID:[http:// | Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domain., Olsen JG, Kadziola A, Lauritzen C, Pedersen J, Larsen S, Dahl SW, FEBS Lett. 2001 Oct 12;506(3):201-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11602245 11602245] | ||
[[Category: Dipeptidyl-peptidase I]] | [[Category: Dipeptidyl-peptidase I]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: tetramer]] | [[Category: tetramer]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:07:09 2008'' | ||
Revision as of 13:07, 20 March 2008
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| , resolution 2.4Å | |||||||
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| Ligands: | , and | ||||||
| Activity: | Dipeptidyl-peptidase I, with EC number 3.4.14.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
dipeptidyl peptidase I (cathepsin C), a tetrameric cysteine protease of the papain family
OverviewOverview
The crystal structure of mature dipeptidyl peptidase I reveals insight into the unique tetrameric structure, substrate binding and activation of this atypical papain family peptidase. Each subunit is composed of three peptides. The heavy and light chains form the catalytic domain, which adopts the papain fold. The residual pro-part forms a beta-barrel with the carboxylate group of Asp1 pointing towards the substrate amino-terminus. The tetrameric structure appears to stabilize the association of the two domains and encloses a 12700 A3 spherical cavity. The tetramer contains six chloride ions, one buried in each S2 pocket and two at subunit interfaces.
About this StructureAbout this Structure
1JQP is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domain., Olsen JG, Kadziola A, Lauritzen C, Pedersen J, Larsen S, Dahl SW, FEBS Lett. 2001 Oct 12;506(3):201-6. PMID:11602245
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